XYNX_ACETH
ID XYNX_ACETH Reviewed; 1087 AA.
AC P38535;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Exoglucanase XynX;
DE EC=3.2.1.91;
DE AltName: Full=1,4-beta-cellobiohydrolase;
DE AltName: Full=Exocellobiohydrolase;
DE Flags: Precursor;
GN Name=xynX;
OS Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium
OS thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=1515;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Pack M.Y., Jung K.H.;
RL Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose
CC and cellotetraose, releasing cellobiose from the non-reducing ends of
CC the chains.; EC=3.2.1.91;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M67438; AAA23227.1; -; Genomic_DNA.
DR PIR; S41797; S41797.
DR AlphaFoldDB; P38535; -.
DR SMR; P38535; -.
DR CAZy; CBM22; Carbohydrate-Binding Module Family 22.
DR CAZy; CBM9; Carbohydrate-Binding Module Family 9.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR PRIDE; P38535; -.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR010502; Carb-bd_dom_fam9.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR001119; SLH_dom.
DR PANTHER; PTHR31490; PTHR31490; 1.
DR Pfam; PF06452; CBM9_1; 2.
DR Pfam; PF02018; CBM_4_9; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR Pfam; PF00395; SLH; 3.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
DR PROSITE; PS51272; SLH; 3.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Repeat; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1087
FT /note="Exoglucanase XynX"
FT /id="PRO_0000007982"
FT DOMAIN 37..188
FT /note="CBM-cenC"
FT DOMAIN 204..527
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT DOMAIN 903..966
FT /note="SLH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT DOMAIN 967..1025
FT /note="SLH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT DOMAIN 1028..1087
FT /note="SLH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT ACT_SITE 347
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 389
FT /evidence="ECO:0000250"
FT ACT_SITE 452
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 1087 AA; 120358 MW; 88077FC27AC83F51 CRC64;
MKNNLSKFVS IFTAFIMIFG TSLFFPHVSA FADDNNANLV SNGDFESGTI DGWIKQGNPT
LAATTEEAIG QYSMKVAGRT QTYEGPAYSF LGKMQKGQSY NVSLKVRLVS GQNSSNPLIT
VTMFREDDNG KHYDTIVWQK QVSEDSWTTV NGTYTLDYTG TLKTLYMYVE SPDPTLEYYI
DDVVVTPQNP IQVGEISNNQ ITIQNDIPDL SSVFKDYFPI GVAVDPSRLN DTDPHAQLTA
KHFNMLVAEN AMKPESLQPT EGNFTFDNAD RIVDYAIAHN MKMRGHTLLW HNQVPDWFFQ
DPSDPTKPAS RDLLLQRLKT HITTVLDHFK TKYGAQNPII GWDVVNEVLD DNGSLRNSKW
LQIIGPDYIE KAFEYAHEAD PSMKLFINDY NIENNGVKTQ AMYDLVKKLK SEGVPISGIG
MQMHININSN IDNIKASIEK LASLGVEIQV TELDMNMNGN VSNEALLKQA RLYKQLFDLF
KAEKQYITAV VFWGVSDDVT WLSKPNAPLL FDSKLQAKPA YWAIADPSKA IPDIQSAKAL
EGSPTIGANV DSSWKLVKPL YANTYVEGTV GATATVKSMW DTKNLYLLVQ VSDNTPSSND
GIEIFVDKND NKSTSYETDD EHYTIKSDGT GSSDITKYVT SNADGYIVQL AIPIEDISPT
LNDKIGLDVR LNDDKGSGSI DTVTVWNDYT NSQDTNTSYF GDIVLSKPAQ VATAIYGTPV
IDGKIDDIWN KVDAITTNTW VLGSDGATAT AKMMWDDKYL YVLADVTDSN LNKSSVNPYE
QDSVEVFVDQ NNDKTSYYES DDGQYRVNYD NEQSFGGSTN SNGFKSATSL TQSGYIVEEA
IPWTSITLLN GTIIGFDLQV NDADENGKRT GIVTWCDPSG NSWQDTSGFG NLLLTGKPSG
VLKKSVTFND IKDNWAKDVI EVLASRHIVE GMTDTQYEPS KTVTRAEFTA MILKLLNIKE
EAYNGEFSDV KNGDWYANAI EAAYKAGIIE GDGKNMRPND SITREEMTSI AMRAYEMLTS
YKEENIGATS FNDDKSISDW AKNVVANAAK LGIINGEPSN VFAPKGIATR AEAAAIIYGL
LEKSNNL